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P14488 (BLAB_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-lactamase 2

EC=3.5.2.6
Alternative name(s):
Beta-lactamase II
Cephalosporinase
Penicillinase
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can hydrolyze carbapenem compounds.

Catalytic activity

A beta-lactam + H2O = a substituted beta-amino acid.

Cofactor

Binds 2 zinc ions per subunit.

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. Class-B beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological_processantibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 256227Beta-lactamase 2
PRO_0000016943

Sites

Metal binding1151Zinc 1 By similarity
Metal binding1171Zinc 1 By similarity
Metal binding1191Zinc 2 By similarity
Metal binding1781Zinc 1 By similarity
Metal binding1971Zinc 2 By similarity
Metal binding2391Zinc 2 By similarity

Experimental info

Mutagenesis1101D → N: No change in activity.
Mutagenesis1191D → N or E: Inactivates the enzyme.
Mutagenesis1771G → E: Inactivates the enzyme.

Sequences

Sequence LengthMass (Da)Tools
P14488 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 670F62378C355C2D

FASTA25628,038
        10         20         30         40         50         60 
MKNTLLKLGV CVSLLGITPF VSTISSVQAE RTVEHKVIKN ETGTISISQL NKNVWVHTEL 

        70         80         90        100        110        120 
GYFSGEAVPS NGLVLNTSKG LVLVDSSWDD KLTKELIEMV EKKFKKRVTD VIITHAHADR 

       130        140        150        160        170        180 
IGGMKTLKER GIKAHSTALT AELAKKNGYE EPLGDLQSVT NLKFGNMKVE TFYPGKGHTE 

       190        200        210        220        230        240 
DNIVVWLPQY QILAGGCLVK SASSKDLGNV ADAYVNEWST SIENVLKRYG NINLVVPGHG 

       250 
EVGDRGLLLH TLDLLK 

« Hide

References

[1]"Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene."
Lim H.M., Pene J.J., Shaw R.W.
J. Bacteriol. 170:2873-2878(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 5/B/6.
[2]"Mutations affecting the catalytic activity of Bacillus cereus 5/B/6 beta-lactamase II."
Lim H.M., Pene J.J.
J. Biol. Chem. 264:11682-11687(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[3]"Site-directed mutagenesis of dicarboxylic acids near the active site of Bacillus cereus 5/B/6 beta-lactamase II."
Lim H.M., Iyer R.K., Pene J.J.
Biochem. J. 276:401-404(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19530 Genomic DNA. Translation: AAA22562.1.
PIRA32017.

3D structure databases

ProteinModelPortalP14488.
SMRP14488. Positions 37-246.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1744488.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP14488.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view]
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
PROSITEPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBLAB_BACCE
AccessionPrimary (citable) accession number: P14488
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families